Melatonin Family Related Drug Discovery Products
Creative Biolabs has the assays you can rely on for high throughput screening, lead optimization, characterizing and discovering targets, and uncovering the complexity of disease pathways. We can offer membrane protein in vitro assay kits that save valuable laboratory time and is ideal for high throughput screening.
Membrane protein stable cell lines are widely used in many areas of biomedical research. Creative Biolabs can offer membrane protein stable cell lines to stablish in vitro models for High Throughput Screening.
Creative Biolabs offers high-quality, innovative tools to help research groups accelerate membrane protein drug discovery. They can be found by targets. If there is no product that meets your needs, please contact us.
Melatonin plays a crucial role in controlling seasonal changes in physiology and neuroendocrine function. Melatonin is processed in the pars tuberalis (PT) of the pituitary and hypothalamus nuclei for these effects. Melatonin has a wide range of accessible receptor subtypes that it can bind to and activate. The MT1 and MT2 subtypes of the melatonin receptor are capable of coupling to several signal transduction cascades. The light/dark cycle, planned arousal, an endogenous pacemaker, melatonin itself, and other hormones are only a few of the stimuli that might control melatonin receptor expression and possibly activity.
Fig.1 Melatonin levels. (Witt-Enderby, 2003)
To meet the needs of melatonin family drug discovery, Creative Biolabs offers a wide variety of in vitro assays and products for our clients:
Overview of Melatonin Family
The MT1 and MT2 receptors are affected by melatonin. The forskolin-stimulated cAMP, protein kinase A signaling, and CREB phosphorylation are inhibited by the MT1 melatonin receptor when it connects to the pertussis toxin-sensitive Gi and -insensitive Gq/11 G proteins. The MT1 receptor also increases potassium conductance through Kir inwardly rectifying channels, as well as the activation of mitogen-activated protein kinase 1/2 and extracellular signal-regulated kinase 1/2. Forskolin-induced cAMP and cGMP synthesis are both inhibited by MT2 melatonin receptor activation, protein kinase C (PKC) is activated in the SCN, and calcium-dependent dopamine release in the retina is decreased.
Additionally, the serotonin (5-HT2C) receptor forms a heterodimer with the MT1 and MT2 receptors. MT2/5-HT2C heterodimer formation is more effective than MT1/5-HT2C heterodimer and 5-HT2C homodimer formation. Melatonin increases the synthesis of inositol phosphate by transactivating the Gq pathway through MT2/5-HT2C heterodimers. Additionally, the development of MT1 and 5-HT2C heterodimeric receptors promotes the trafficking of 5-HT2C receptors to the cell surface and enhances the recruitment of β-arrestin triggered by melatonin and 5-HT. Therefore, when novel melatonin-like medicines are created, it is important to investigate how the melatonin receptor heterodimerizes with the 5-HT2C receptor and perhaps other receptor types to produce additional signaling responses with therapeutic promise.
Fig.2 Signaling schematic of melatonin receptor subtypes. (Slominski, 2012)
Melatonin Family Drug Discovery
Molecular and genetic techniques must be used to identify melatonin receptor expression and their physiological roles in health and disease. With regard to immunomodulation, endocrine function regulation, anti-cancer activity, circadian activity, cardiovascular activity, skin pigmentation, hair growth, and aging, these receptors are desirable targets for pharmaceuticals. So, increasing our understanding of how melatonin receptors are expressed, regulated, signaled, and function in peripheral cells and tissues may have an effect on the pharmacotherapy of a variety of diseases.
References
- Witt-Enderby, P.A.; et al. Melatonin receptors and their regulation: biochemical and structural mechanisms. Life sciences. 2003, 72(20): 2183-2198.
- Slominski, R.M.; et al. Melatonin membrane receptors in peripheral tissues: distribution and functions. Molecular and cellular endocrinology. 2012, 351(2): 152-166.
